Cite

Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G.,. Gudmundsson G.H,: FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc. Natl. Acad. Sci. USA. 92, 195–199 (1995) Agerberth B. Gunne H. Odeberg J. Kogner P. Boman H.G. ,. Gudmundsson G.H, FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis Proc. Natl. Acad. Sci. USA. 92 195 199 199510.1073/pnas.92.1.195428447529412 Search in Google Scholar

Agier J., Brzezińska-Błaszczyk E.: Katelicydyny i defensyny w regulacji aktywności przeciwdrobnoustrojowej komórek tucznych. Post. Hig. Med. Dośw. 70, 618–636 (2016) Agier J. Brzezińska-Błaszczyk E. Katelicydyny i defensyny w regulacji aktywności przeciwdrobnoustrojowej komórek tucznych Post. Hig. Med. Dośw. 70 618 636 201610.5604/17322693.120535727333932 Search in Google Scholar

Agier J., Efenberger M., Brzezińska-Błaszczyk E.: Cathelicidin impact on inflammatory cells. Centr. Eur. J. Immunol. 40, 225–235 (2015) Agier J. Efenberger M. Brzezińska-Błaszczyk E. Cathelicidin impact on inflammatory cells Centr. Eur. J. Immunol. 40 225 235 201510.5114/ceji.2015.51359463738426557038 Search in Google Scholar

Albrethsen J., Møller C. H., Olsen J., Raskov H., Gammeltoft S.: Human neutrophil peptides 1, 2 and 3 are biochemical markers for metastatic colorectal cancer. Eur. J. Cancer, 42, 3057–3064 (2006) Albrethsen J. Møller C. H. Olsen J. Raskov H. Gammeltoft S. Human neutrophil peptides 1, 2 and 3 are biochemical markers for metastatic colorectal cancer Eur. J. Cancer 42 3057 3064 200610.1016/j.ejca.2006.05.03917015013 Search in Google Scholar

Amer L.S., Bishop B.M., van Hoek M.L.: Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella. Biochem. Biophys. Res. Commun. 396, 246–251 (2010) Amer L.S. Bishop B.M. van Hoek M.L. Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella Biochem. Biophys. Res. Commun. 396 246 251 201010.1016/j.bbrc.2010.04.07320399752 Search in Google Scholar

Andersson E., Sorensen O.E., Frohm B., Borregaard N., Egesten A., Malm J.: Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes. Hum. Reprod. 17, 2529–2534 (2002) Andersson E. Sorensen O.E. Frohm B. Borregaard N. Egesten A. Malm J. Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes Hum. Reprod. 17 2529 2534 200210.1093/humrep/17.10.252912351523 Search in Google Scholar

Antimicrobial peptide datebase: http://aps.unmc.edu/AP/main.php (6.02.2018) Antimicrobial peptide datebase http://aps.unmc.edu/AP/main.php (6.02.2018) Search in Google Scholar

Bagnicka E., Strzałkowska N., Jóźwik A., Horbańczuk J.O., Krzyżewski J., Zwierzchowski L.: Peptydy przeciwdrobnoustrojowe w zwalczaniu patogenów opornych na powszechnie stosowane antybiotyki. Medycyna Wet. 67, 512–516 (2011) Bagnicka E. Strzałkowska N. Jóźwik A. Horbańczuk J.O. Krzyżewski J. Zwierzchowski L. Peptydy przeciwdrobnoustrojowe w zwalczaniu patogenów opornych na powszechnie stosowane antybiotyki Medycyna Wet. 67 512 516 2011 Search in Google Scholar

Bagnicka E., Strzałkowska N., Jóźwik A., Krzyżewski J., Horbańczuk J., Zwierzchowski L.: Expression and polymorphism of defensins in farm animals. Acta Bioch. Pol. 4, 487–497 (2010) Bagnicka E. Strzałkowska N. Jóźwik A. Krzyżewski J. Horbańczuk J. Zwierzchowski L. Expression and polymorphism of defensins in farm animals Acta Bioch. Pol. 4 487 497 201010.18388/abp.2010_2434 Search in Google Scholar

Bals R., Lang C., Weiner D.J., Vogelmeier C., Welsch U., Wilson J.M.: Rhesus monkey (Macaca mulatta) mucosal antibacterial peptides are close homologues of human molecules. Clin. Diagnost. Lab. Immunol. 8, 370–375 (2001) Bals R. Lang C. Weiner D.J. Vogelmeier C. Welsch U. Wilson J.M. Rhesus monkey (Macaca mulatta) mucosal antibacterial peptides are close homologues of human molecules Clin. Diagnost. Lab. Immunol. 8 370 375 200110.1128/CDLI.8.2.370-375.20019606511238224 Search in Google Scholar

Bals R., Wang X., Zasloff M., Wilson J.M.: The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc. Natl. Acad. Sci. USA 95, 9541–9546 (1998) Bals R. Wang X. Zasloff M. Wilson J.M. The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface Proc. Natl. Acad. Sci. USA 95 9541 9546 199810.1073/pnas.95.16.9541213749689116 Search in Google Scholar

Barlow P.G., Li Y., Wilkinson T.S., Bowdish D.M.E., Lau Y.E., Cosseau C., Haslett C., Simpson A.J., Hancock R.E., Davidson D.J.: The human cationic host defense peptide LL-37 mediates contrasting effects on apoptotic pathways in different primary cells of the innate immune system. J. Leuk. Biol. 80, 509–520 (2006) Barlow P.G. Li Y. Wilkinson T.S. Bowdish D.M.E. Lau Y.E. Cosseau C. Haslett C. Simpson A.J. Hancock R.E. Davidson D.J. The human cationic host defense peptide LL-37 mediates contrasting effects on apoptotic pathways in different primary cells of the innate immune system J. Leuk. Biol. 80 509 520 200610.1189/jlb.1005560185155116793910 Search in Google Scholar

Benincasa M., Scocchi M., Pacor S., Tossi A., Nobili D., Basaglia G., Busetti M., Gennaro R.: Fungicidal activity of five cathelicidin peptides agains clinically isolated yeasts. J. Antimicrob. Chemother. 58, 950–959 (2006) Benincasa M. Scocchi M. Pacor S. Tossi A. Nobili D. Basaglia G. Busetti M. Gennaro R. Fungicidal activity of five cathelicidin peptides agains clinically isolated yeasts J. Antimicrob. Chemother. 58 950 959 200610.1093/jac/dkl38217023499 Search in Google Scholar

Bergman P., Johansson L., Asp V., Plant L., Gudmundsson G.H., Jonsson A.B., Agerberth B.: Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37. Cell. Microbiol. 7, 1009–1017 (2005) Bergman P. Johansson L. Asp V. Plant L. Gudmundsson G.H. Jonsson A.B. Agerberth B. Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37 Cell. Microbiol. 7 1009 1017 200510.1111/j.1462-5822.2005.00530.x15953032 Search in Google Scholar

Bowdish, D. M., Davidson D.J., Lau Y.E., Lee K., Scott M.G., Hancock R.E., Bowdish D.M.: Impact of LL-37 on anti-infective immunity. J. Leuk. Biol. 77, 451–459 (2005) Bowdish D. M. Davidson D.J. Lau Y.E. Lee K. Scott M.G. Hancock R.E. Bowdish D.M. Impact of LL-37 on anti-infective immunity J. Leuk. Biol. 77 451 459 200510.1189/jlb.070438015569695 Search in Google Scholar

Braff M.H., Bardan A., Nizet V., Gallo R.L.: Cutaneous defense mechanisms by antimicrobial peptides. J. Invest. Dermatol. 125, 9–13 (2005) Braff M.H. Bardan A. Nizet V. Gallo R.L. Cutaneous defense mechanisms by antimicrobial peptides J. Invest. Dermatol. 125 9 13 200510.1111/j.0022-202X.2004.23587.x15982297 Search in Google Scholar

Brogden K.A., Ackermann M., McCray P.B. jr.: Antimicrobial peptides in animals and their role in host defences. Int. J. Antimicrobial Agents, 22, 465–478 (2003) Brogden K.A. Ackermann M. McCray P.B. jr. Antimicrobial peptides in animals and their role in host defences Int. J. Antimicrobial Agents 22 465 478 200310.1016/S0924-8579(03)00180-8 Search in Google Scholar

Brown K.L., Hancock R.E.W.: Cationic host defense (antimicrobial) peptides. Curr. Opinion Immunol. 18, 24–30 (2006) Brown K.L. Hancock R.E.W. Cationic host defense (antimicrobial) peptides Curr. Opinion Immunol. 18 24 30 200610.1016/j.coi.2005.11.00416337365 Search in Google Scholar

Chang CI., Zhang Y.A., Zou J., Nie P., Secombes C.J.: Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and atlantic salmon (Salmo salar). Antomicrob. Agents Chemother, 50, 185–195 (2006) Chang CI. Zhang Y.A. Zou J. Nie P. Secombes C.J. Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and atlantic salmon (Salmo salar) Antomicrob. Agents Chemother 50 185 195 200610.1128/AAC.50.1.185-195.2006134676916377685 Search in Google Scholar

Chen H., Takai T., Xie Y., Niyonsaba F., Okumura K., Ogawa H.: Human antimicrobial peptide LL-37 modulates proinflammatory responses induced by cytokine milieus and double-stranded RNA in human keratinocytes. Biochem. Biophys. Res. Commun. 433, 532–537 (2013) Chen H. Takai T. Xie Y. Niyonsaba F. Okumura K. Ogawa H. Human antimicrobial peptide LL-37 modulates proinflammatory responses induced by cytokine milieus and double-stranded RNA in human keratinocytes Biochem. Biophys. Res. Commun. 433 532 537 201310.1016/j.bbrc.2013.03.02423524263 Search in Google Scholar

Cole A.M.: Innate host defense of human vaginal and cervical mucosae. Curr. Top. Microbiol. Immunol. 306, 199–230 (2006) Cole A.M. Innate host defense of human vaginal and cervical mucosae Curr. Top. Microbiol. Immunol. 306 199 230 200610.1097/01.lgt.0000265775.52044.2b Search in Google Scholar

Conner K., Nern K., Rudisill J., O’Grady T, Gallo R.L.: The antimicrobial pepitide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris. J. Am. Acad. Dermatol. 47, 347–350 (2002) Conner K. Nern K. Rudisill J. O’Grady T Gallo R.L. The antimicrobial pepitide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris J. Am. Acad. Dermatol. 47 347 350 200210.1067/mjd.2002.12219012196742 Search in Google Scholar

Cubeddu T., Cacciotto C., Pisanu S., Tedde V., Alberti A., Pittau M., Dore S., Cannas A., Uzzau S., Rocca S., Addis M.F.: Cathelicidin production and release by mammary epithelial cells during infectious mastitis. Vet. Immunol. Immunopathol. 189, 66–70 (2017) Cubeddu T. Cacciotto C. Pisanu S. Tedde V. Alberti A. Pittau M. Dore S. Cannas A. Uzzau S. Rocca S. Addis M.F. Cathelicidin production and release by mammary epithelial cells during infectious mastitis Vet. Immunol. Immunopathol. 189 66 70 201710.1016/j.vetimm.2017.06.00228669389 Search in Google Scholar

Dean S.N., Bishop B.M., van Hoek M.L.: Susceptibility of Pseudomonas aeruginosa biofilm to alpha-helical peptides: D-enantiomer of LL-37. Front. Microbiol. 2, http://dx.doi.org/10.3389/fmicb.2011.00128 (2011) Dean S.N. Bishop B.M. van Hoek M.L. Susceptibility of Pseudomonas aeruginosa biofilm to alpha-helical peptides: D-enantiomer of LL-37 Front. Microbiol. 2 http://dx.doi.org/10.3389/fmicb.2011.00128 201110.3389/fmicb.2011.00128313151921772832 Search in Google Scholar

Di Na, Vitiello A., Gallo R.L.: Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide. J. Immunol. 170, 2274–2278 (2003) Di Na Vitiello A. Gallo R.L. Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide J. Immunol. 170 2274 2278 200310.4049/jimmunol.170.5.227412594247 Search in Google Scholar

Dorschner R.A., Pestonjamasp V.K., Tamakuwala S., Ohtake T., Rudisill J., Nizet V., Agerberth B., Gudmundsson G.H., Gallo R.L.: Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J. Invest. Dermatol. 117, 91–97 (2001) Dorschner R.A. Pestonjamasp V.K. Tamakuwala S. Ohtake T. Rudisill J. Nizet V. Agerberth B. Gudmundsson G.H. Gallo R.L. Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus J. Invest. Dermatol. 117 91 97 200110.1046/j.1523-1747.2001.01340.x11442754 Search in Google Scholar

Dosler S., Karaaslan E.: Inhibition and destruction of Pseudomonas aureginosa biofilms by antibiotics and antimicrobial peptides. Peptides, 62, 32–37 (2014) Dosler S. Karaaslan E. Inhibition and destruction of Pseudomonas aureginosa biofilms by antibiotics and antimicrobial peptides Peptides 62 32 37 201410.1016/j.peptides.2014.09.02125285879 Search in Google Scholar

Dürr U.H.N., Sudheendra U.S., Ramamoorthy A.: LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta, 1758, 1408–1425 (2006) Dürr U.H.N. Sudheendra U.S. Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides Biochim. Biophys. Acta 1758 1408 1425 200610.1016/j.bbamem.2006.03.03016716248 Search in Google Scholar

Erdag G.: Interleukin- 1α and interleukin – 6 enhance the antibacterial properties of cultured composite keratinocyte grafts. Ann. Surg. 235, 113–124 (2002) Erdag G. Interleukin- 1α and interleukin – 6 enhance the antibacterial properties of cultured composite keratinocyte grafts Ann. Surg. 235 113 124 200210.1097/00000658-200201000-00015142240311753050 Search in Google Scholar

Ericksen B., Wu Z., Lu W., Lehrer R.I.. Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob. Agents Chemother. 49, 269–275, (2005) Ericksen B. Wu Z. Lu W. Lehrer R.I. Antibacterial activity and specificity of the six human {alpha}-defensins Antimicrob. Agents Chemother. 49 269 275 200510.1128/AAC.49.1.269-275.200553887715616305 Search in Google Scholar

Feliucio M.R., Silva O.N., Goncalves S., Santos N.C., Franco O.L.: Peptides with dual antimicrobial and anticancer activities. Front Chem. Feb 21, 5:5. Doi: 10.3389/fchem.2017.00005. eCollection 2017 (2017) Feliucio M.R. Silva O.N. Goncalves S. Santos N.C. Franco O.L. Peptides with dual antimicrobial and anticancer activities Front Chem Feb 21 5 5 Doi: 10.3389/fchem.2017.00005 eCollection 2017 2017531846328271058 Open DOISearch in Google Scholar

Findlay E.G., Currie S.M., Davidson D.J.: Cationic host defence peptides: potential as antiviral therapeutics. Biodrugs, 27, 479–493 (2013) Findlay E.G. Currie S.M. Davidson D.J. Cationic host defence peptides: potential as antiviral therapeutics Biodrugs 27 479 493 201310.1007/s40259-013-0039-0377515323649937 Search in Google Scholar

Frohm N., Sandstedt B., Sorensen O., Weber G., Borregaard N., Stahle-Backdahl M.: The human cationic antimicrobial protein (hCAP-18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6. Inf. Immunity, 67, 2561–2566 (1999) Frohm N. Sandstedt B. Sorensen O. Weber G. Borregaard N. Stahle-Backdahl M. The human cationic antimicrobial protein (hCAP-18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6 Inf. Immunity 67 2561 2566 199910.1128/IAI.67.5.2561-2566.199911600410225921 Search in Google Scholar

Gallo R.l., Hooper L.V.: Epithelial antimicrobail defence of the skin and intestine. Nat. Rev. Immunol. 12, 503–516 (2012) Gallo R.l. Hooper L.V. Epithelial antimicrobail defence of the skin and intestine Nat. Rev. Immunol. 12 503 516 201210.1038/nri3228356333522728527 Search in Google Scholar

Gorman S.P., Glimore B.F.: Clinical relevance of the escape pathogens. Expert Rev. Anti-infect. Ther. 11, 297–308 (2013) Gorman S.P. Glimore B.F. Clinical relevance of the escape pathogens Expert Rev. Anti-infect. Ther. 11 297 308 201310.1586/eri.13.1223458769 Search in Google Scholar

Hancock R.E.W., Haney E.F., Gill E.E.: The immunology of host defence peptides: Beyond antimicrobial activity. Nat. Rev. Immunol. 16, 321–334 (2016) Hancock R.E.W. Haney E.F. Gill E.E. The immunology of host defence peptides: Beyond antimicrobial activity Nat. Rev. Immunol. 16 321 334 201610.1038/nri.2016.2927087664 Search in Google Scholar

Hase K., Eckmann L., Leopard J.D., Varki N., Kagnoff M.F.: Cell differentiation is a key determionant of cathelicidin LL-37/human cationic antimicrobial protein 18 expresion by human colon ephitelium. Infect. Immunity, 70, 953–963 (2002) Hase K. Eckmann L. Leopard J.D. Varki N. Kagnoff M.F. Cell differentiation is a key determionant of cathelicidin LL-37/human cationic antimicrobial protein 18 expresion by human colon ephitelium Infect. Immunity 70 953 963 200210.1128/IAI.70.2.953-963.200212771711796631 Search in Google Scholar

Hazlett L., Wu M.: Defensins in innate immunity. Cell Tissue Res. 343, 175–188 (2011) Hazlett L. Wu M. Defensins in innate immunity Cell Tissue Res. 343 175 188 201110.1007/s00441-010-1022-420730446 Search in Google Scholar

Hell É., Giske C.G., Nelson A., Römling U., Marchini G.: Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis. Lett. Appl. Microbiol. 50, 211–215 (2010) Hell É. Giske C.G. Nelson A. Römling U. Marchini G. Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis Lett. Appl. Microbiol. 50 211 215 201010.1111/j.1472-765X.2009.02778.x20002576 Search in Google Scholar

Henning-Pauka J., Jacobsen I., Blecha F.: Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleura pneumonias infection. Vet. Res. 37, 75–87 (2006) Henning-Pauka J. Jacobsen I. Blecha F. Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleura pneumonias infection Vet. Res. 37 75 87 200610.1051/vetres:200504316336926 Search in Google Scholar

Hu Z., Murakami T., Suzuki K., Tamura H., Kawahara-Arai K., Ilba T., Nagoaka I.: Antimicrobial cathelicidin peptide LL-37 inhibits the LPS/ATP-induced pyroptosis of macrophages by dual mechanism. PLoS ONE 9, p.e85765 (2014) Hu Z. Murakami T. Suzuki K. Tamura H. Kawahara-Arai K. Ilba T. Nagoaka I. Antimicrobial cathelicidin peptide LL-37 inhibits the LPS/ATP-induced pyroptosis of macrophages by dual mechanism PLoS ONE 9 p.e85765 201410.1371/journal.pone.0085765389420724454930 Search in Google Scholar

Huang W., Seo J., Willingham S.B., Gonzalgo M.L., Weissman I.L., Barron A.E.: Cationic, amphipathic peptides with potent anticancer activity. PLoS ONE 9, e90397. Huang W. Seo J. Willingham S.B. Gonzalgo M.L. Weissman I.L. Barron A.E. Cationic, amphipathic peptides with potent anticancer activity PLoS ONE 9 e90397 10.1371/journal.pone.0090397393872324587350 Search in Google Scholar

Hurtado P., Peh C. A.: LL-37 promotes rapid sensing of CpG oligodeoxynucleotides by B lymphocytes and plasmacytoid dendritic cells. J. Immunol. 184, 1425–1435 (2010) Hurtado P. Peh C. A. LL-37 promotes rapid sensing of CpG oligodeoxynucleotides by B lymphocytes and plasmacytoid dendritic cells J. Immunol. 184 1425 1435 201010.4049/jimmunol.090230520042575 Search in Google Scholar

Into T., Inomata M., Shibata K., Murakami Y.: Effect of the antimcirobial peptide LL-37 on Toll-like receptors 2-,3- and 4-triggered expression of IL-6, IL-8 and CXCL10 in human gingival fibroblasts. Cell Immunol 264, 104–109 (2010) Into T. Inomata M. Shibata K. Murakami Y. Effect of the antimcirobial peptide LL-37 on Toll-like receptors 2-,3- and 4-triggered expression of IL-6, IL-8 and CXCL10 in human gingival fibroblasts Cell Immunol 264 104 109 201010.1016/j.cellimm.2010.05.00520570250 Search in Google Scholar

Jarczak J., Kościuczuk E.M., Lisowski P., Strzałkowska N., Jóźwik A., Horbańczuk J., Krzyżewski J., Zwierzchwoski L., Bagnicka E.: Defensins: natural komponent of human innate immunity. Hum. Immunol. 74, 1069–1079 (2013) Jarczak J. Kościuczuk E.M. Lisowski P. Strzałkowska N. Jóźwik A. Horbańczuk J. Krzyżewski J. Zwierzchwoski L. Bagnicka E. Defensins: natural komponent of human innate immunity Hum. Immunol. 74 1069 1079 201310.1016/j.humimm.2013.05.00823756165 Search in Google Scholar

Jones E.A., Cheng Y., O’Meally D., Belov K.: Characterization of the antimicrobial peptide family defensins in the Tasmanian devil (sarcophilus harrissi), koala (Phasco9larctos cinereus), and tammar wallaby (macropus eugenii). Immunogenetics, 69, 133–143 (2017) Jones E.A. Cheng Y. O’Meally D. Belov K. Characterization of the antimicrobial peptide family defensins in the Tasmanian devil (sarcophilus harrissi), koala (Phasco9larctos cinereus), and tammar wallaby (macropus eugenii) Immunogenetics 69 133 143 201710.1007/s00251-016-0959-127838759 Search in Google Scholar

Klotman M.E., Chang T.L.: Defensin in innate antiviral immunity. Nat. Rev. Immunol. 6, 447–456 (2006) Klotman M.E. Chang T.L. Defensin in innate antiviral immunity Nat. Rev. Immunol. 6 447 456 200610.1038/nri186016724099 Search in Google Scholar

Kościuczuk E.M., Lisowski P., Jarczak J., Strzałkowska N., Jóźwik A., Horbończuk J., Krzyżewski J., Zwierzechowski L., Bagnicka E.: Cathelicidins: family of antimicrobial peptides. Mol. Biol. Rep. 39, 10957–10970 (2012) Kościuczuk E.M. Lisowski P. Jarczak J. Strzałkowska N. Jóźwik A. Horbończuk J. Krzyżewski J. Zwierzechowski L. Bagnicka E. Cathelicidins: family of antimicrobial peptides Mol. Biol. Rep. 39 10957 10970 201210.1007/s11033-012-1997-x348700823065264 Search in Google Scholar

Kurashima Y., Kiyono H.: Mucosal ecological network of epithelium and immune cells for gut homeostasis and tissue healing. Annu. Res. Immunol. 35, 119–241 (2017) Kurashima Y. Kiyono H. Mucosal ecological network of epithelium and immune cells for gut homeostasis and tissue healing Annu. Res. Immunol. 35 119 241 201710.1146/annurev-immunol-051116-05242428125357 Search in Google Scholar

Lai Y., Adhikurakunnathu S., Bhardaj K., Ranjith-Kumar C.T., Wen Y., Jordan J.L., Wu L.H., Dragnea B., San Mateo L., Kao C.C.: LL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAs. PLoS ONE, 6, e26632 (2011) Lai Y. Adhikurakunnathu S. Bhardaj K. Ranjith-Kumar C.T. Wen Y. Jordan J.L. Wu L.H. Dragnea B. San Mateo L. Kao C.C. LL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAs PLoS ONE 6 e26632 201110.1371/journal.pone.0026632319878622039520 Search in Google Scholar

Larrick J.W., Hirata M., Zhong J., Wright S.C.: Anti-microbial activity of human CAP18 peptides. Immunotechnology, 1, 65–72 (1995) Larrick J.W. Hirata M. Zhong J. Wright S.C. Anti-microbial activity of human CAP18 peptides Immunotechnology 1 65 72 199510.1016/1380-2933(95)00006-29373334 Search in Google Scholar

Laube D.M., Yim S., Ryan L.K., Kisich K.O., Diamond G.: Antimicrobial peptides in the airway. Curr. Top. Microbiol. Immunol. 306, 153–182 (2006) Laube D.M. Yim S. Ryan L.K. Kisich K.O. Diamond G. Antimicrobial peptides in the airway Curr. Top. Microbiol. Immunol. 306 153 182 200610.1007/3-540-29916-5_616909921 Search in Google Scholar

Lee M.O., Jang H.J., Rengaraj D., Yang S.Y., Han S.Y., Lamont S.J., Womack J.E.: Tissue expression and antibacterial activity of host defense peptides in chicken. BMC Vet. Res. 12, 231–239 (2016) Lee M.O. Jang H.J. Rengaraj D. Yang S.Y. Han S.Y. Lamont S.J. Womack J.E. Tissue expression and antibacterial activity of host defense peptides in chicken BMC Vet. Res. 12 231 239 201610.1186/s12917-016-0866-6506490727737668 Search in Google Scholar

Lehrer R.I.: Primate defensin. Nat. Rev. Microbiol. 2, 727–738 (2004) Lehrer R.I. Primate defensin Nat. Rev. Microbiol. 2 727 738 200410.1038/nrmicro97615372083 Search in Google Scholar

Li J., Koh J.J., Liu S., Lakshminarayanan R., Verma C.S., Beuerman R.W.: Membrane active antomicrobial peptides: translating mechanistic insights to design. Front. Neurosci. 11, 73–98 (2017) Li J. Koh J.J. Liu S. Lakshminarayanan R. Verma C.S. Beuerman R.W. Membrane active antomicrobial peptides: translating mechanistic insights to design Front. Neurosci. 11 73 98 2017 Search in Google Scholar

Linde A., Ross C.R., Davis E.G., Dib L., Blecha F., Melgarejo T.: Innate Immunity and host defense peptides in veterinary medicine. J. Vet. Intern. Med. 22, 247–265 (2008) Linde A. Ross C.R. Davis E.G. Dib L. Blecha F. Melgarejo T. Innate Immunity and host defense peptides in veterinary medicine J. Vet. Intern. Med. 22 247 265 200810.1111/j.1939-1676.2007.0038.x18312280 Search in Google Scholar

Lopez-Garcia B., Lee P.H.A., Gallo R.L.: Expresion and potential function of cathelicidin antimicrobial peptides in dermatophytosis and tinea versicolor. J. Antimicrob. Chemother. 57, 877–882 (2006) Lopez-Garcia B. Lee P.H.A. Gallo R.L. Expresion and potential function of cathelicidin antimicrobial peptides in dermatophytosis and tinea versicolor J. Antimicrob. Chemother. 57 877 882 200610.1093/jac/dkl07816556635 Search in Google Scholar

Luo Y., McLean D.T.F., Linden G,J., McAuley D.F., McMullan R., Lundy F.T.: The naturally occurring host defense peptide, LL-37, and its truncated mimetics KE-18 and KR-12 have selected biocidal and antibiofilm activities against Candida albicans, Staphylococcus aureus, and Escherichia coli in vitro. Front. Microbiol. 8, 1–11 (2017) Luo Y. McLean D.T.F. Linden G,J. McAuley D.F. McMullan R. Lundy F.T. The naturally occurring host defense peptide, LL-37, and its truncated mimetics KE-18 and KR-12 have selected biocidal and antibiofilm activities against Candida albicans, Staphylococcus aureus, and Escherichia coli in vitro Front. Microbiol. 8 1 11 201710.3389/fmicb.2017.00544537421928408902 Search in Google Scholar

Coorens M., Schneider V.A.F., de Groot A.M., van Dijk A., Meijerink M., Wells J.M., Scheenstra M.R., Veldhuizen E.J.A., Haagsman H.P.: Cathelicidins inhibit Escherichia coli – induced TLR2 and TLR4 activation in a viability-dependent manner. J. Immunol. 199, 1418–1428 (2017) Coorens M. Schneider V.A.F. de Groot A.M. van Dijk A. Meijerink M. Wells J.M. Scheenstra M.R. Veldhuizen E.J.A. Haagsman H.P. Cathelicidins inhibit Escherichia coli – induced TLR2 and TLR4 activation in a viability-dependent manner J. Immunol. 199 1418 1428 201710.4049/jimmunol.1602164554493128710255 Search in Google Scholar

Mansour S.C., Pena O.M., Hancock R.E.W.: Host defense peptides: front-line immunomodulators. Trends. Immunol. 39, 443–450 (2014) Mansour S.C. Pena O.M. Hancock R.E.W. Host defense peptides: front-line immunomodulators Trends. Immunol. 39 443 450 201410.1016/j.it.2014.07.00425113635 Search in Google Scholar

Marchini G., Lindow S., Brismar H., Stabi B., Berggren V., Ulfgren A.K., Lonne-Rahm S., Agerberth B., Gudmundsson G.H.: The newborn infant is protected by an innate antimicrobial barrier: peptide antibiotics are present in the skin and vernix caseosa. Br. J. Dermatol. 147, 1127–1134 (2002) Marchini G. Lindow S. Brismar H. Stabi B. Berggren V. Ulfgren A.K. Lonne-Rahm S. Agerberth B. Gudmundsson G.H. The newborn infant is protected by an innate antimicrobial barrier: peptide antibiotics are present in the skin and vernix caseosa Br. J. Dermatol. 147 1127 1134 200210.1046/j.1365-2133.2002.05014.x12452861 Search in Google Scholar

Midorikawa K., Ouhara K., Komatsuzawa H., Kawai T., Yamada S., Fujiwara T., Yamazaki K., Sayama K., Taubman M.A., Kurihara H., Hashimoto K., Sugai M.: Staphylococcus aureus susceptibility to innate antimicrobial peptides, beta-defensins and CAP18, expressed by human keratinocytes. Inf. Immunity, 71, 3730–3739 (2003) Midorikawa K. Ouhara K. Komatsuzawa H. Kawai T. Yamada S. Fujiwara T. Yamazaki K. Sayama K. Taubman M.A. Kurihara H. Hashimoto K. Sugai M. Staphylococcus aureus susceptibility to innate antimicrobial peptides, beta-defensins and CAP18, expressed by human keratinocytes Inf. Immunity 71 3730 3739 200310.1128/IAI.71.7.3730-3739.200316200212819054 Search in Google Scholar

Mirski T., Gryko R., Bartoszcze M., Bielawska-Drozd A., Tyszkiewicz W.: Peptydy przeciwdrobnoustrojowe – nowe możliwości zwalczania infekcji u ludzi i zwierząt. Medycyna Wet. 67, 517–521 (2011) Mirski T. Gryko R. Bartoszcze M. Bielawska-Drozd A. Tyszkiewicz W. Peptydy przeciwdrobnoustrojowe – nowe możliwości zwalczania infekcji u ludzi i zwierząt Medycyna Wet. 67 517 521 2011 Search in Google Scholar

Mizerska-Dudka M., Andrejko M., Kandafer-Szerszeń M.: Przeciwwirusowe peptydy kationowe człowieka i owadów. Post. Mikrobiol. 50, 209–216 (2011) Mizerska-Dudka M. Andrejko M. Kandafer-Szerszeń M. Przeciwwirusowe peptydy kationowe człowieka i owadów Post. Mikrobiol. 50 209 216 2011 Search in Google Scholar

Murakami M., Ohtake T., Dorschner R.A., Gallo R.L.: Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. J. Dent. Res. 81, 845–850 (2002) Murakami M. Ohtake T. Dorschner R.A. Gallo R.L. Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva J. Dent. Res. 81 845 850 200210.1177/15440591020810121012454100 Search in Google Scholar

Murakami M., Ohtake T., Dorschner R.A., Schittek B., Garbe C., Gallo R.L.: Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin. J. Invest. Dermatol. 119, 1090–1095 (2002) Murakami M. Ohtake T. Dorschner R.A. Schittek B. Garbe C. Gallo R.L. Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin J. Invest. Dermatol. 119 1090 1095 200210.1046/j.1523-1747.2002.19507.x12445197 Search in Google Scholar

Nagaoka I., Tamura H., Hirata M.: An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formyl-peptide receptor-like 1 and P2X7. J. Immunol. 176, 3044–3052 (2006) Nagaoka I. Tamura H. Hirata M. An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formyl-peptide receptor-like 1 and P2X7 J. Immunol. 176 3044 3052 200610.4049/jimmunol.176.5.304416493063 Search in Google Scholar

Niedźwiedzka-Rystwej P., Deptuła W.: Defensyny – ważny wrodzony element układu odpornościowego u ssaków. Post. Hig. Med. Dośw. 62, 524–529 (2008) Niedźwiedzka-Rystwej P. Deptuła W. Defensyny – ważny wrodzony element układu odpornościowego u ssaków Post. Hig. Med. Dośw. 62 524 529 2008 Search in Google Scholar

Niedźwiedzka-Rystwej P., Mękal A., Deptuła W.: Peptydy przeciwdrobnoustrojowe – ważny element odporności naturalnej. Astma Alergia Immunol. 15, 35–41 (2010) Niedźwiedzka-Rystwej P. Mękal A. Deptuła W. Peptydy przeciwdrobnoustrojowe – ważny element odporności naturalnej Astma Alergia Immunol. 15 35 41 2010 Search in Google Scholar

Nijnik, A., Hancock, R. E. W. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr. Opin. Hematol. 16, 41–47 (2009) Nijnik, A. Hancock R. E. W. The roles of cathelicidin LL-37 in immune defences and novel clinical applications Curr. Opin. Hematol. 16 41 47 200910.1097/MOH.0b013e32831ac517 Search in Google Scholar

Nijnik, A., Pistolic, J., Filewod, N.C.J., Hancock, R. E. W.: Signaling pathways mediating chemokine induction in keratinocytes by cathelicidin LL-37 and flagellin. J. Innate Immun. 4, 377–386 (2012) Nijnik A. Pistolic J. Filewod N.C.J. Hancock R. E. W. Signaling pathways mediating chemokine induction in keratinocytes by cathelicidin LL-37 and flagellin J. Innate Immun. 4 377 386 201210.1159/000335901674162822516952 Search in Google Scholar

Ong P.Y., Ohtake T., Brandt C et al.: Endogenous antimicrobial peptides and skin infections in atopic dermatitis. N. Engl. J. Med. 347, 1151–1160 (2002) Ong P.Y. Ohtake T. Brandt C Endogenous antimicrobial peptides and skin infections in atopic dermatitis N. Engl. J. Med. 347 1151 1160 200210.1056/NEJMoa02148112374875 Search in Google Scholar

Oppenheim J.J., Yang D.: Alarmins: chemotactic activators of immune response. Curr. Opin. Immunol. 17, 359–365 (2005) Oppenheim J.J. Yang D. Alarmins: chemotactic activators of immune response Curr. Opin. Immunol. 17 359 365 200510.1016/j.coi.2005.06.00215955682 Search in Google Scholar

Polcyn-Adamczyk M., Niemir Z.I.: Katelicydyna – budowa, funkcja i rola w chorobach autoimmunologicznych. Post. Biol. Kom. 41, 315–330 (2014) Polcyn-Adamczyk M. Niemir Z.I. Katelicydyna – budowa, funkcja i rola w chorobach autoimmunologicznych Post. Biol. Kom. 41 315 330 2014 Search in Google Scholar

Pomorska-Mól M., Markowska-Daniel I.: Katelicydyny i defensyny u świń. Medycyna Wet. 67, 20–24 (2011) Pomorska-Mól M. Markowska-Daniel I. Katelicydyny i defensyny u świń Medycyna Wet. 67 20 24 2011 Search in Google Scholar

Porcelli F., Verardi R., Shi L., Henzler-Wildman K.A., Ramamorthny A., Veglia G.: NMR structure of the cathelicidin-derived human antimicribal peptide LL-37 in dodecylphosphocholine micelles. Biochemistry, 47, 5565–5572 (2008) Porcelli F. Verardi R. Shi L. Henzler-Wildman K.A. Ramamorthny A. Veglia G. NMR structure of the cathelicidin-derived human antimicribal peptide LL-37 in dodecylphosphocholine micelles Biochemistry 47 5565 5572 200810.1021/bi702036s587359018439024 Search in Google Scholar

Ramanathan B., davis E.G., Ross C.R., Blecha F.: Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect. 4, 361–372 (2002) Ramanathan B. davis E.G. Ross C.R. Blecha F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity Microbes Infect. 4 361 372 200210.1016/S1286-4579(02)01549-611909747 Search in Google Scholar

Ritonja A., Kopitar R., Jerela R., Turk V.: Primary structure of a new cysteine proteinase inhibitor from pig leukocytes. FEBS Leters, 255, 211–214 (1989) Ritonja A. Kopitar R. Jerela R. Turk V. Primary structure of a new cysteine proteinase inhibitor from pig leukocytes FEBS Leters 255 211 214 198910.1016/0014-5793(89)81093-22792375 Search in Google Scholar

Rivas-Santiago B., Hernandez-Pando R., Carranza C., Juarez E., Contreras J.L., Aguilar-Leon D., Torres M., Sada E.: Expression of cathelicidin LL-37 during Mycobacterium tuberculosis infection in human alveolar macrophages, monocytes, neutrophils, and epithelial cells. Infect. Immun. 76, 935–941 (2008) Rivas-Santiago B. Hernandez-Pando R. Carranza C. Juarez E. Contreras J.L. Aguilar-Leon D. Torres M. Sada E. Expression of cathelicidin LL-37 during Mycobacterium tuberculosis infection in human alveolar macrophages, monocytes, neutrophils, and epithelial cells Infect. Immun. 76 935 941 200810.1128/IAI.01218-07225880118160480 Search in Google Scholar

Robinson K., Deng Z., Hou Y., Zhang G.: Regulation of the intestinal barrier function by host defense peptides. Front. Vet. Sci. doi:0.3389/fvets.2015.00057 (2015) Robinson K. Deng Z. Hou Y. Zhang G. Regulation of the intestinal barrier function by host defense peptides Front. Vet. Sci doi:0.3389/fvets.2015.00057 2015 Open DOISearch in Google Scholar

Schaller-Bals S., Schulze A., Bals R.: Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am. J. Respir. Crit. Care. Med. 165, 992–995 (2002) Schaller-Bals S. Schulze A. Bals R. Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection Am. J. Respir. Crit. Care. Med. 165 992 995 200210.1164/ajrccm.165.7.200110-02011934727 Search in Google Scholar

Scott M.G., Hancock R.E.: Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit. Rev. Immunol. 20, 407–431 (2000) Scott M.G. Hancock R.E. Cationic antimicrobial peptides and their multifunctional role in the immune system Crit. Rev. Immunol 20 407 431 200010.1615/CritRevImmunol.v20.i5.40 Search in Google Scholar

Seil M., Nagant C., Dehaye J.P., Vandenbranden M., Lensink M.F.: Spothlight on human LL-37, an immunomodulatory peptide with promising cell- penetrating properties. Pharmaceuticals. 3, 3435–3460 (2010) Seil M. Nagant C. Dehaye J.P. Vandenbranden M. Lensink M.F. Spothlight on human LL-37, an immunomodulatory peptide with promising cell- penetrating properties Pharmaceuticals 3 3435 3460 201010.3390/ph3113435 Search in Google Scholar

Selsted M.E., Harwig S.S., Ganz T., Schilling J.W., Lehrer R.I. Primary structures of three human neutrophil defensins. J. Clin. Invest. 76, 1436–1439 (1985) Selsted M.E. Harwig S.S. Ganz T. Schilling J.W. Lehrer R.I. Primary structures of three human neutrophil defensins J. Clin. Invest. 76 1436 1439 198510.1172/JCI1121214240954056036 Search in Google Scholar

Selsted M.E., Novotny M.J., Morris W.L., Tang Y.Q., Smith W., Cullor J.S.: Indfolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J.Biol. Chem. 267, 4292–4295 (1992) Selsted M.E. Novotny M.J. Morris W.L. Tang Y.Q. Smith W. Cullor J.S. Indfolicidin, a novel bactericidal tridecapeptide amide from neutrophils J.Biol. Chem 267 4292 4295 199210.1016/S0021-9258(18)42830-X Search in Google Scholar

Selsted M.E., Ouellette A.J.: Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551–557 (2005) Selsted M.E. Ouellette A.J. Mammalian defensins in the antimicrobial immune response Nat. Immunol 6 551 557 200510.1038/ni120615908936 Search in Google Scholar

Sima P., Trebichavsky I., Sigler K.: Mammalian antibiotic peptides. Folia Microbiol. (Praha), 48, 123–137 (2003) Sima P. Trebichavsky I. Sigler K. Mammalian antibiotic peptides Folia Microbiol. (Praha) 48 123 137 200310.1007/BF0293094512800493 Search in Google Scholar

Skerlavaj B., Scocchi M., Gennaro R., Risso A., Zanetti M.: Structural and functionsal analysis of horse cathelicidin peptides. Antimicrob. Agents Chemother. 45, 715–722 (2001) Skerlavaj B. Scocchi M. Gennaro R. Risso A. Zanetti M. Structural and functionsal analysis of horse cathelicidin peptides Antimicrob. Agents Chemother. 45 715 722 200110.1128/AAC.45.3.715-722.20019036211181349 Search in Google Scholar

Śliwa-Dominiak J., Witkowska M., Deptuła W.: Biologiczne alternatywy dla antybiotyków. Przegl. Epidemiol. 64, 399–403 (2010) Śliwa-Dominiak J. Witkowska M. Deptuła W. Biologiczne alternatywy dla antybiotyków Przegl. Epidemiol 64 399 403 2010 Search in Google Scholar

Smeianov V., Scott K., Reid G.: Activity of cecropin P1 and FA-LL-37 against urogenital microflora. Microbes Infect. 2, 773–777 (2000) Smeianov V. Scott K. Reid G. Activity of cecropin P1 and FA-LL-37 against urogenital microflora Microbes Infect. 2 773 777 200010.1016/S1286-4579(00)90359-910955957 Search in Google Scholar

Sonawane A., Santos J.C., Mishra B.B., Jena P., Progida C., Sorensen O.E., Gallo R., Appelberg R., Groffiths G.: Cathelicidin is involved in the intracellular killing of mycobacteria in macrophages:the role of cathelicidin in mycobacteria killing. Cell. Microbiol. 13, 1601–1617 (2013) Sonawane A. Santos J.C. Mishra B.B. Jena P. Progida C. Sorensen O.E. Gallo R. Appelberg R. Groffiths G. Cathelicidin is involved in the intracellular killing of mycobacteria in macrophages:the role of cathelicidin in mycobacteria killing Cell. Microbiol. 13 1601 1617 201310.1111/j.1462-5822.2011.01644.x21790937 Search in Google Scholar

Sőrensen O.E., Borregaard N., Cole A.M.: Antimicrobial peptides in innate immune responses. Contrib. Microbiol. 15, 61–77 (2008) Sőrensen O.E. Borregaard N. Cole A.M. Antimicrobial peptides in innate immune responses Contrib. Microbiol 15 61 77 200810.1159/00013631518511856 Search in Google Scholar

Steiner H., Hultmark D., Engström Å., Bennich H., Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature, 292, 246–248 (1981) Steiner H. Hultmark D. Engström Å. Bennich H. Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity Nature 292 246 248 198110.1038/292246a07019715 Search in Google Scholar

Thomma B.P., Cammue B.P., Thevissen K.: Plant defensins. Planta, 216, 193–202 (2002) Thomma B.P. Cammue B.P. Thevissen K. Plant defensins Planta 216 193 202 200210.1007/s00425-002-0902-612447532 Search in Google Scholar

Tomasinsig L., Conti G., Skerljavaj B., Piccinini R., Mazzilli M., D’Este F., Tossi A., Zanetti M.: Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary ephitelial cells support s ptotective role of neutrophil cathelicidins in bovine mastisis. Inf. Immun. 78, 1781–1788 (2010) Tomasinsig L. Conti G. Skerljavaj B. Piccinini R. Mazzilli M. D’Este F. Tossi A. Zanetti M. Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary ephitelial cells support s ptotective role of neutrophil cathelicidins in bovine mastisis Inf. Immun. 78 1781 1788 201010.1128/IAI.01090-09284941920100862 Search in Google Scholar

Tomasinsig L., Zanetti M.: The cathelicidins – structure, functions and evolution. Curr. Protein. Pept. Sci. 6, 23–34 (2005) Tomasinsig L. Zanetti M. The cathelicidins – structure, functions and evolution Curr. Protein. Pept. Sci 6 23 34 200510.2174/138920305302752015638766 Search in Google Scholar

Treffers C., Chen L., Anderson R.C., Yu P.L.: Isolation and characterisation of antimicrobial peptides from deer neutrophils. Int. J. Antomicrob. Agents. 26, 165–169 (2005) Treffers C. Chen L. Anderson R.C. Yu P.L. Isolation and characterisation of antimicrobial peptides from deer neutrophils Int. J. Antomicrob. Agents. 26 165 169 200510.1016/j.ijantimicag.2005.05.00116011891 Search in Google Scholar

Turner J., Cho Y., Dinh N.N., Waring A.J., Lehrer R.I.: Activities of LL-37, a cathelinassociated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42, 2206–2214 (1998) Turner J. Cho Y. Dinh N.N. Waring A.J. Lehrer R.I. Activities of LL-37, a cathelinassociated antimicrobial peptide of human neutrophils Antimicrob. Agents Chemother. 42 2206 2214 199810.1128/AAC.42.9.22061057789736536 Search in Google Scholar

Uzzell T., Stolzenberg E.D., Shinnar A.E., Zasloff M.: Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides, 24, 1655–1667 (2003) Uzzell T. Stolzenberg E.D. Shinnar A.E. Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins Peptides 24 1655 1667 200310.1016/j.peptides.2003.08.02415019197 Search in Google Scholar

Van Dijk A., Veldhuizen E.J., van Asten A.J., Haagsman H.P.: CMAP27, a novel chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway. Proc. Natl. Acad. Sci. USA, 104, 15063–15068 (2005) Van Dijk A. Veldhuizen E.J. van Asten A.J. Haagsman H.P. CMAP27, a novel chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway Proc. Natl. Acad. Sci. USA 104 15063 15068 2005 Search in Google Scholar

Vandamme D., Landuyt B., Luyten W., Schoofs L: A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell Immunol. 280, 22–35 (2012) Vandamme D. Landuyt B. Luyten W. Schoofs L A comprehensive summary of LL-37, the factotum human cathelicidin peptide Cell Immunol. 280 22 35 201210.1016/j.cellimm.2012.11.00923246832 Search in Google Scholar

Wang Y., Hong J., Liu X., Yang H., Liu R., Wu J., Wang A., Lin D., Lai R.: Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS ONE 3, e3217. Wang Y. Hong J. Liu X. Yang H. Liu R. Wu J. Wang A. Lin D. Lai R. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics PLoS ONE 3 e3217 10.1371/journal.pone.0003217252893618795096 Search in Google Scholar

Wang G., Li X., Wang Z.: APD3: the antimicrobial peptide database as a tool for reaserch and education. Nucleic Acids Res. 44, 1087–1093 (2016) Wang G. Li X. Wang Z. APD3: the antimicrobial peptide database as a tool for reaserch and education Nucleic Acids Res. 44 1087 1093 201610.1093/nar/gkv1278470290526602694 Search in Google Scholar

Wang G, Watson K.M., Buckheit R.W. Jr.: Anti-human immunodeficiency voirus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. Antimicrob. Agents Chemother. 52, 3438–3440 (2008) Wang G Watson K.M. Buckheit R.W. Jr. Anti-human immunodeficiency voirus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins Antimicrob. Agents Chemother 52 3438 3440 200810.1128/AAC.00452-08253347618591279 Search in Google Scholar

Wangl Y., Walter G., Herting E., Agerberth B.,. Johansson J.: Antibacterial activities of the cathelicidins prophenin (residues 63 to 79) and LL-37 in the presence of a lung surfactant preparation. Antimicrob. Agents Chemother. J. 48, 2097–2100 (2004) Wangl Y. Walter G. Herting E. Agerberth B. ,. Johansson J. Antibacterial activities of the cathelicidins prophenin (residues 63 to 79) and LL-37 in the presence of a lung surfactant preparation Antimicrob. Agents Chemother. J. 48 2097 2100 200410.1128/AAC.48.6.2097-2100.200441558915155206 Search in Google Scholar

Wiechuła B.E., Tustanowski J.P., Martirosian G.: Peptydy antybrobnoustrojowe. Wiad. Lek. 59, 542–547 (2006) Wiechuła B.E. Tustanowski J.P. Martirosian G. Peptydy antybrobnoustrojowe Wiad. Lek. 59 542 547 2006 Search in Google Scholar

Witkowska D., Bartyś A., Gamian A.: Defensyny i katelicydyny jako naturalne antybiotyki peptydowe. Post. Hig. Med. Dośw. 62, 694–707 (2008) Witkowska D. Bartyś A. Gamian A. Defensyny i katelicydyny jako naturalne antybiotyki peptydowe Post. Hig. Med. Dośw. 62 694 707 2008 Search in Google Scholar

Wódz K., Brzezińska-Błaszczyk E.: Katelicydyny – endogenne peptydy przeciwdrobnoustrojowe. Post. Biochemii, 61, 93–101 (2015) Wódz K. Brzezińska-Błaszczyk E. Katelicydyny – endogenne peptydy przeciwdrobnoustrojowe Post. Biochemii 61 93 101 2015 Search in Google Scholar

Wu H., Zhang G., Minton J.E., Ross C.R., Blecha F.: Regulation of cathelicidin gene expresie: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serowar typhimurium infection. Infect. Immunity, 68, 5552–5558 (2000) Wu H. Zhang G. Minton J.E. Ross C.R. Blecha F. Regulation of cathelicidin gene expresie: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serowar typhimurium infection Infect. Immunity 68 5552 5558 200010.1128/IAI.68.10.5552-5558.200010150510992453 Search in Google Scholar

Xhindoli D., Pacor S., Beninscasa M., Scocchi M., Gennaro R., Tossi A.: The human cathelicidin LL-37 – a pore-forming antibacterial peptide and host-cell modulator. Biochim. Biophis. Acta, 1858, 546–566 (2016) Xhindoli D. Pacor S. Beninscasa M. Scocchi M. Gennaro R. Tossi A. The human cathelicidin LL-37 – a pore-forming antibacterial peptide and host-cell modulator Biochim. Biophis. Acta 1858 546 566 201610.1016/j.bbamem.2015.11.00326556394 Search in Google Scholar

Xiao Y, Cai Y., Bommineni Y.R., Femando S.C., Prakash O., Gilliland S.E., Zhang G.: Identifikation and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 281, 2858–2867 (2006) Xiao Y Cai Y. Bommineni Y.R. Femando S.C. Prakash O. Gilliland S.E. Zhang G. Identifikation and functional characterization of three chicken cathelicidins with potent antimicrobial activity J. Biol. Chem. 281 2858 2867 200610.1074/jbc.M50718020016326712 Search in Google Scholar

Yamasaki K., Schauber J., Coda A., Lin H., Dorschner R.A., Schechter N.M., Bonnart C., Descargues P., Hovnanian A., Gallo R.L.: Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. FASEB J. 20, 2068–2080 (2006) Yamasaki K. Schauber J. Coda A. Lin H. Dorschner R.A. Schechter N.M. Bonnart C. Descargues P. Hovnanian A. Gallo R.L. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin FASEB J. 20 2068 2080 200610.1096/fj.06-6075com17012259 Search in Google Scholar

Yang D., de la Rosa G., Tewary P., Oppenheim J.J.: Alarmins link neutrophils and dendritic cells. Trends Immunol. 30, 531–537 (2009) Yang D. de la Rosa G. Tewary P. Oppenheim J.J. Alarmins link neutrophils and dendritic cells Trends Immunol. 30 531 537 200910.1016/j.it.2009.07.004276743019699678 Search in Google Scholar

Zanetti M.: The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 17, 179–196 (2005) Zanetti M. The role of cathelicidins in the innate host defenses of mammals Curr. Issues Mol. Biol. 17 179 196 2005 Search in Google Scholar

Zasloff M.: Antimicrobial peptides of multucellular organisms. Nature, 415, 389–395 (2002) Zasloff M. Antimicrobial peptides of multucellular organisms Nature 415 389 395 200210.1038/415389a11807545 Search in Google Scholar

Zasloff M.: Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA, 84, 5449–5453 (1987) Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor Proc. Natl. Acad. Sci. USA 84 5449 5453 198710.1073/pnas.84.15.54492988753299384 Search in Google Scholar

Zea H.I., Spitznagel J.K.: Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identifications. Science, 142, 1085–1087 (1963) Zea H.I. Spitznagel J.K. Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identifications Science 142 1085 1087 196310.1126/science.142.3595.108514068232 Search in Google Scholar

Żelechowska P., Agier J., Brzezińska-Błaszczak E.: Endogenous antimicrobial factors in the treatment of infectious diseases. Cent. Europ. J. Immunol. 41, 419–425 (2016) Żelechowska P. Agier J. Brzezińska-Błaszczak E. Endogenous antimicrobial factors in the treatment of infectious diseases Cent. Europ. J. Immunol. 41 419 425 201610.5114/ceji.2016.65141538288728450805 Search in Google Scholar

Żyłowska M., Wyszyńska A., Jagusztyn-Krynicka K.: Defensyny – peptydy o aktywności przeciwbakteryjnej. Post. Mikrobiol. 50, 223–234 (2011) Żyłowska M. Wyszyńska A. Jagusztyn-Krynicka K. Defensyny – peptydy o aktywności przeciwbakteryjnej Post. Mikrobiol 50 223 234 2011 Search in Google Scholar

eISSN:
2545-3149
Languages:
English, Polish
Publication timeframe:
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Journal Subjects:
Life Sciences, Microbiology and Virology